l-Alanine binding sites and Na+, K+-ATPase in cilia and other membrane fractions from olfactory rosettes of Atlantic salmon
Document Type
Article
Date of Original Version
1-1-1991
Abstract
1. 1. Membrane fractions were obtained from homogenates of olfactory rosettes from Atlantic salmon (Salmo salar) or from isolated olfactory cilia and homogenates of deciliated olfactory rosettes. 2. 2.|Specific binding of l-[3H]alanine was saturable, high-affinity, and effectively inhibited by l-threonine, l-serine and l-alanine but not by l-lysine or l-glutamic acid. Comparable results were obtained with l[3H]serine except for the presence of a second, lower affinity, binding site for l-alanine but not l-serine. 3. 3. Specific binding of l[3H]alanine was inhibited by low concentrations of mercury ion, acidic pH, and high concentrations of cadmium, copper or zinc ions. Aluminum had no effect. 4. 4. Specific binding sites for l-alanine were present in membranes from isolated cilia at a level 2-fold that of membranes prepared from the deciliated rosette. 5. 5. Ouabain sensitive Na+, K+-ATPase activity was also determined in cilia preparations. This enzyme was present in cilia at a level approximately 3-fold that of membranes prepared from the deciliated rosette. 6. 6.|The results are consistent with the presence of an olfactory alanine receptor in S. salar with binding characteristics similar to those of a variety of other fish species and with a localization on olfactory cilia as well as non-ciliated receptor cell membranes. © 1991.
Publication Title, e.g., Journal
Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume
98
Issue
1
Citation/Publisher Attribution
Lo, Ying Har, Terence M. Bradley, and Dennis E. Rhoads. "l-Alanine binding sites and Na+, K+-ATPase in cilia and other membrane fractions from olfactory rosettes of Atlantic salmon." Comparative Biochemistry and Physiology -- Part B: Biochemistry and 98, 1 (1991). doi: 10.1016/0305-0491(91)90317-7.